ID   A0A1H3AZ96_9PSEU        Unreviewed;       290 AA.
AC   A0A1H3AZ96;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Citrate lyase subunit beta / citryl-CoA lyase {ECO:0000313|EMBL:SDX35052.1};
GN   ORFNames=SAMN05421504_1021122 {ECO:0000313|EMBL:SDX35052.1};
OS   Amycolatopsis xylanica.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Amycolatopsis.
OX   NCBI_TaxID=589385 {ECO:0000313|EMBL:SDX35052.1, ECO:0000313|Proteomes:UP000199515};
RN   [1] {ECO:0000313|EMBL:SDX35052.1, ECO:0000313|Proteomes:UP000199515}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CPCC 202699 {ECO:0000313|EMBL:SDX35052.1,
RC   ECO:0000313|Proteomes:UP000199515};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR   EMBL; FNON01000002; SDX35052.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H3AZ96; -.
DR   STRING; 589385.SAMN05421504_1021122; -.
DR   OrthoDB; 9768429at2; -.
DR   Proteomes; UP000199515; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   InterPro; IPR005000; Aldolase/citrate-lyase_domain.
DR   InterPro; IPR011206; Citrate_lyase_beta/mcl1/mcl2.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   PANTHER; PTHR32308:SF10; CITRATE LYASE SUBUNIT BETA; 1.
DR   PANTHER; PTHR32308; LYASE BETA SUBUNIT, PUTATIVE (AFU_ORTHOLOGUE AFUA_4G13030)-RELATED; 1.
DR   Pfam; PF03328; HpcH_HpaI; 1.
DR   PIRSF; PIRSF015582; Cit_lyase_B; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE   4: Predicted;
KW   Lyase {ECO:0000313|EMBL:SDX35052.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR015582-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR015582-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199515}.
FT   DOMAIN          8..222
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   BINDING         69
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         127
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         127
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         154
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   290 AA;  30853 MW;  B4FBF1E4364814F2 CRC64;
     MTELRPRRSV LYMPGANERA LEKAKGLDAD ALILDLEDAV APDAKEAARE RVCAAASSGD
     YGRREVTIRV NGLDTAWHDA DLRAAAQAGP AAVVVPKVNS AAEVHNIERA LELGGAPDHT
     KIWAMVETPI AMLHAEEIAA ASERLTVLVM GTNDLAKELH AEFVPGRAPL LGGLSLALLA
     ARATGKVILD GVYNDVKDLE GFEAECVQGR QFGFDGKTLI HPGQLEACNR VFAPSAEEIE
     RSEKIIAAFE TAQAEGRGVV TVDGRMIENL HVDNARRVLA LADAIGKAGD
//